ID Q1LN93_CUPMC Unreviewed; 118 AA. AC Q1LN93; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 91. DE RecName: Full=Ribulose bisphosphate carboxylase small subunit {ECO:0000256|HAMAP-Rule:MF_00859}; DE Short=RuBisCO small subunit {ECO:0000256|HAMAP-Rule:MF_00859}; GN Name=cbbS {ECO:0000256|HAMAP-Rule:MF_00859, GN ECO:0000313|EMBL:ABF08383.1}; GN OrderedLocusNames=Rmet_1500 {ECO:0000313|EMBL:ABF08383.1}; OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / OS CH34) (Ralstonia metallidurans). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF08383.1, ECO:0000313|Proteomes:UP000002429}; RN [1] {ECO:0000313|Proteomes:UP000002429} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34 RC {ECO:0000313|Proteomes:UP000002429}; RX PubMed=20463976; DOI=10.1371/journal.pone.0010433; RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A., RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C., RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.; RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a RT master survivalist in harsh and anthropogenic environments."; RL PLoS ONE 5:E10433-E10433(2010). CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide CC fixation, as well as the oxidative fragmentation of the pentose CC substrate. Both reactions occur simultaneously and in competition at CC the same active site. Although the small subunit is not catalytic it is CC essential for maximal activity. {ECO:0000256|HAMAP-Rule:MF_00859}. CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits. CC {ECO:0000256|HAMAP-Rule:MF_00859}. CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO CC this homodimer is arranged in a barrel-like tetramer with the small CC subunits forming a tetrameric 'cap' on each end of the 'barrel'. CC {ECO:0000256|HAMAP-Rule:MF_00859}. CC -!- SIMILARITY: Belongs to the RuBisCO small chain family. CC {ECO:0000256|HAMAP-Rule:MF_00859}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000352; ABF08383.1; -; Genomic_DNA. DR RefSeq; WP_011516246.1; NC_007973.1. DR AlphaFoldDB; Q1LN93; -. DR STRING; 266264.Rmet_1500; -. DR KEGG; rme:Rmet_1500; -. DR eggNOG; COG4451; Bacteria. DR HOGENOM; CLU_098114_2_0_4; -. DR Proteomes; UP000002429; Chromosome. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule. DR CDD; cd03527; RuBisCO_small; 1. DR Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 1. DR HAMAP; MF_00859; RuBisCO_S_bact; 1. DR InterPro; IPR024681; RuBisCO_ssu. DR InterPro; IPR000894; RuBisCO_ssu_dom. DR InterPro; IPR036385; RuBisCO_ssu_sf. DR PANTHER; PTHR31262; RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC; 1. DR Pfam; PF00101; RuBisCO_small; 1. DR SMART; SM00961; RuBisCO_small; 1. DR SUPFAM; SSF55239; RuBisCO, small subunit; 1. PE 3: Inferred from homology; KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP- KW Rule:MF_00859}; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_00859}; Lyase {ECO:0000313|EMBL:ABF08383.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002429}. FT DOMAIN 18..115 FT /note="Ribulose bisphosphate carboxylase small subunit" FT /evidence="ECO:0000259|SMART:SM00961" SQ SEQUENCE 118 AA; 13661 MW; A303A4DCF7AE1677 CRC64; MSDVMDYNSR LSDPASRKFE TFSYLPAMDA ASIKRQVEYL VKKGWNPAIE HIEPEYLMDS YWYMWKLPMF GETDVDRVLA EAKACHKANP NNHVRLVGYD NFKQSQGAAM VVYRGKTV //